1TSR: P53 core domain

P53 core domain in complex with DNA. Determined by X-ray diffraction at 2.2 Å resolution. Released 29 Jan 1996.

Method: X-ray diffraction
Resolution: 2.2 Å
Organism: Homo sapiens
Chains: 5
Atoms: 5,828
Mol. weight: 86.84 kDa
Ligands: ZN
Released: 29 Jan 1996

Explore 1TSR in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1TSR contains 16 α-helices and 37 β-strands across 3 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 5 helices, 13 β-strands

Element	Residues	Length	Sheet
β-strand	103	1	1
β-strand	110-112	3	2
β-strand	124-127	4	1
β-strand	132-135	4	1
β-strand	141-146	6	2
α-helix	150-152	3
β-strand	156-163	8	1
α-helix	166-168	3
β-strand	172	1	1
α-helix	173	1
α-helix	177-180	4
β-strand	195-198	4	2
β-strand	204-207	4	1
β-strand	214-219	6	1
β-strand	230-236	7	2
β-strand	251-258	8	1
β-strand	264-274	11	1
α-helix	278-287	10

Chain B: 4 helices, 12 β-strands

Element	Residues	Length	Sheet
β-strand	103	1	3
β-strand	110-112	3	4
β-strand	124-127	4	3
β-strand	132-135	4	3
β-strand	141-146	6	4
β-strand	156-163	8	3
α-helix	167-170	4
α-helix	177-181	5
β-strand	195-198	4	4
β-strand	204-207	4	3
β-strand	214-219	6	3
α-helix	222-224	3
β-strand	230-236	7	4
β-strand	251-258	8	3
β-strand	264-274	11	3
α-helix	278-287	10

Chain C: 7 helices, 12 β-strands

Element	Residues	Length	Sheet
β-strand	103	1	5
α-helix	105-107	3
β-strand	110-112	3	6
β-strand	125-127	3	5
β-strand	132-136	5	5
β-strand	141-146	6	6
α-helix	151-152	2
β-strand	156-163	8	5
α-helix	166-169	4
α-helix	172-173	2
α-helix	177-180	4
β-strand	195-197	3	6
β-strand	204-207	4	5
β-strand	214-219	6	5
α-helix	222-224	3
β-strand	230-236	7	6
β-strand	251-258	8	5
β-strand	264-275	12	5
α-helix	278-285	8

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
DNA (5'-d(tptptpcpcptpapgpapcptptpgpcpcpcpa paptptp*a)-3')	E	DNA	21
DNA (5'-d(aptpapaptptpgpgpgpcpapapgptpcptpa pgpgpap*a)-3')	F	DNA	21
Protein (P53 tumor suppressor)	A, B, C	protein	219	Homo sapiens	P04637 (AlphaFold model)

Sequence of entity 1 (E), FASTA

>1TSR_1 DNA (5'-D(*TP*TP*TP*CP*CP*TP*AP*GP*AP*CP*TP*TP*GP*CP*CP*CP*A P*AP*TP*TP*A)-3') (chains E)
TTTCCTAGACTTGCCCAATTA

Sequence of entity 2 (F), FASTA

>1TSR_2 DNA (5'-D(*AP*TP*AP*AP*TP*TP*GP*GP*GP*CP*AP*AP*GP*TP*CP*TP*A P*GP*GP*AP*A)-3') (chains F)
ATAATTGGGCAAGTCTAGGAA

Sequence of entity 3 (A, B, C), FASTA

>1TSR_3 PROTEIN (P53 TUMOR SUPPRESSOR) (chains A, B, C)
SSSVPSQKTYQGSYGFRLGFLHSGTAKSVTCTYSPALNKMFCQLAKTCPVQLWVDSTPPP
GTRVRAMAIYKQSQHMTEVVRRCPHHERCSDSDGLAPPQHLIRVEGNLRVEYLDDRNTFR
HSVVVPYEPPEVGSDCTTIHYNYMCNSSCMGGMNRRPILTIITLEDSSGNLLGRNSFEVR
VCACPGRDRRTEEENLRKKGEPHHELPPGSTKRALPNNT

Ligands and cofactors

ID	Name	Formula	Copies
ZN	Zinc ion	Zn	3

Primary citation

Crystal structure of a p53 tumor suppressor-DNA complex: understanding tumorigenic mutations. Cho, Y., Gorina, S., Jeffrey, P.D. et al. Science (1994) 265:346-355. PubMed

Other PDB entries of the same protein (UniProt P04637 (AlphaFold model), which also has an AlphaFold model), best resolution first:

9C5S 1.01 Å, Disulfide-linked, antiparallel p53-derived peptide dimer (CV1)
3D06 1.2 Å, Human p53 core domain with hot spot mutation R249S (I)
5MHC 1.2 Å, Crystal structure of 14-3-3sigma and a p53 C-terminal 12-mer synthetic phosphopeptide
8UQR 1.22 Å, Crystal structure of the human p53 tetramerization domain
6GGC 1.24 Å, p53 cancer mutant Y220C in complex with small-molecule stabilizer PK9320
6SHZ 1.24 Å, p53 cancer mutant Y220C
4MZI 1.25 Å, Crystal structure of a human mutant p53
6GGE 1.25 Å, p53 cancer mutant Y220C in complex with small-molecule stabilizer PK9327
3LW1 1.28 Å, Binary complex of 14-3-3 sigma and p53 pT387-peptide
5O1E 1.3 Å, p53 cancer mutant Y220C im complex with compound MB577
6RL3 1.3 Å, Fragment AZ-003 binding at the p53pT387/14-3-3 sigma interface
8E7A 1.3 Å, Crystal structure of the p53 (Y107H) core domain orthorhombic P form

Browse structure collections

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